B: Biopolymer transport protein ExbB C: Biopolymer transport protein ExbB D: Biopolymer transport protein ExbB E: Biopolymer transport protein ExbB F: Biopolymer transport protein ExbB G: Biopolymer transport protein ExbB H: Biopolymer transport protein ExbB I: Biopolymer transport protein ExbB J: Biopolymer transport protein ExbB A: Biopolymer transport protein ExbB hetero molecules
B: Biopolymer transport protein ExbB C: Biopolymer transport protein ExbB D: Biopolymer transport protein ExbB F: Biopolymer transport protein ExbB A: Biopolymer transport protein ExbB hetero molecules
E: Biopolymer transport protein ExbB G: Biopolymer transport protein ExbB H: Biopolymer transport protein ExbB I: Biopolymer transport protein ExbB J: Biopolymer transport protein ExbB hetero molecules
Mass: 18.015 Da / Num. of mol.: 142 / Source method: isolated from a natural source / Formula: H2O
Compound details
Authors state that all of the experiments indicate that ExbD is present in the structure, but not ...Authors state that all of the experiments indicate that ExbD is present in the structure, but not well ordered. The density for it is not good enough to build into. This happens at neutral pH. However, at low pH, the ExbD helix can be seen clearly. Authors hypothesize that since this complex responds to the proton motive force (proton gradient), the order of the ExbD helix is modulated by pH.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 4.07 Å3/Da / Density % sol: 69.8 %
Crystal grow
Temperature: 288 K / Method: vapor diffusion, hanging drop Details: 100 mM HEPES-NaOH, pH 7.0, 100 mM CaCl2, and 22% PEG MME 550
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1 Å / Relative weight: 1
Reflection
Resolution: 2.6→46 Å / Num. obs: 126321 / % possible obs: 96.3 % / Redundancy: 3.5 % / Rsym value: 0.12 / Net I/σ(I): 14.1
Reflection shell
Resolution: 2.6→2.69 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.9 / Mean I/σ(I) obs: 1.2 / % possible all: 95.7
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Processing
Software
Name
Version
Classification
PHENIX
(1.10_2142: ???)
refinement
DENZO
HKL2000
datareduction
SCALEPACK
HKL2000
datascaling
PHASER
PHENIX
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→46 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 30.39 Details: Authors state that all of the experiments indicate that ExbD is present in the structure, but not well ordered. The density for it is not good enough to build into. This happens at neutral ...Details: Authors state that all of the experiments indicate that ExbD is present in the structure, but not well ordered. The density for it is not good enough to build into. This happens at neutral pH. However, at low pH, the ExbD helix can be seen clearly. Authors hypothesize that since this complex responds to the proton motive force (proton gradient), the order of the ExbD helix is modulated by pH.